The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.
Structural Mechanisms Underlying Posttranslational Modification by Ubiquitin-Like Proteins
Abstract
Covalent attachment of ubiquitin-like proteins (Ubls) is a predominant mechanism for regulating protein function in eukaryotes. Several structurally related Ubls, such as ubiquitin, SUMO, NEDD8, and ISG15, modify a vast number of proteins, altering their functions in a variety of ways. Ubl modifications can affect the target's half-life, subcellular localization, enzymatic activity, or ability to interact with protein or DNA partners. Generally, these diverse Ubls are covalently attached via their C termini to their targets by parallel, but specific, cascades involving three classes of enzymes known as E1, E2, and E3. Structures are now available for many protein complexes in E1-E2-E3 cascades, revealing a series of modular building blocks and providing mechanistic insights into their functions.
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Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G.-L., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,198
Function and regulation of cullin–RING ubiquitin ligases
Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148
The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,054
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O'Rourke, K. M., Zhou, H., Eby, M., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,856
Structure of ubiquitin refined at 1.8 Å resolution
Vijay-kumar, S., Bugg, C. E., & Cook, W. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,742
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,716
Johnson, E. S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074118 · Cited by 1,675
A proteomics approach to understanding protein ubiquitination
Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., & Gygi, S. P. (2003) · Nature Biotechnology · doi:10.1038/nbt849 · Cited by 1,602
Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins
Kerscher, O., Felberbaum, R., & Hochstrasser, M. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010605.093503 · Cited by 1,517
Cited by
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy
Hanada, T., Noda, N. N., Satomi, Y., Ichimura, Y., Fujioka, Y., Takao, T., Inagaki, F., & Ohsumi, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700195200 · Cited by 1,123
The emerging complexity of protein ubiquitination
Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821
Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767
Self-citationStructural insights into the catalysis and regulation of E3 ubiquitin ligases
Buetow, L., & Huang, D. T. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.91 · Cited by 679
Metadata
- Authors
- Dye, B. T., & Schulman, B. A.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 2007-06-01
- Volume
- 36
- Issue
- 1
- Pages
- 131-150
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2103210708
- Cited by
- 264
- References
- 105
- FWCI
- 7.78
- Type
- journal article
- Language
- en
- Open access
- closed
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- Dye, B. T., & Schulman, B. A. (2007). Structural Mechanisms Underlying Posttranslational Modification by Ubiquitin-Like Proteins. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.36.040306.132820
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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